scholarly journals Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion

2012 ◽  
Vol 197 (6) ◽  
pp. 819-836 ◽  
Author(s):  
Fangliang Zhang ◽  
Sougata Saha ◽  
Anna Kashina
Keyword(s):  
Cell Adhesion ◽  
Cell Attachment ◽  
Adhesion Formation ◽  
Cell Matrix ◽  
Intracellular Regulation ◽  
Dependent Cell ◽  
Cell Matrix Adhesion ◽  
Proteolytic Product ◽  
Cell Cell

Talin is a large scaffolding molecule that plays a major role in integrin-dependent cell–matrix adhesion. A role for talin in cell–cell attachment through cadherin has never been demonstrated, however. Here, we identify a novel calpain-dependent proteolytic cleavage of talin that results in the release of a 70-kD C-terminal fragment, which serves as a substrate of posttranslational arginylation. The intracellular levels of this fragment closely correlated with the formation of cell–cell adhesions, and this fragment localized to cadherin-containing cell–cell contacts. Moreover, reintroduction of this fragment rescued the cell–cell adhesion defects in arginyltransferase (Ate1) knockout cells, which normally have a very low level of this fragment. Arginylation of this fragment further enhanced its ability to rescue cell–cell adhesion formation. In addition, arginylation facilitated its turnover, suggesting a dual role of arginylation in its intracellular regulation. Thus, our work identifies a novel proteolytic product of talin that is regulated by arginylation and a new role of talin in cadherin-dependent cell–cell adhesion.

Cdk5 regulates cell-matrix and cell-cell adhesion in lens epithelial cells

2002 ◽  
Vol 115 (10) ◽  
pp. 2109-2117 ◽  
Author(s):  
Sewite Negash ◽  
Hwai-Shi Wang ◽  
Chun Gao ◽  
Dolena Ledee ◽  
Peggy Zelenka
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Cell Attachment ◽  
Dominant Negative ◽  
Lens Epithelial Cells ◽  
Fiber Cells ◽  
Cell Matrix ◽  
Dominant Negative Mutation ◽  
Cell Cell

Cdk5 is a member of the cyclin-dependent kinase family, which is expressed predominantly in terminally differentiated neurons. Lower levels of Cdk5 are also found in a wide variety of cell types, including the lens. Although Cdk5 has been shown to play an important role in neuronal migration and neurite outgrowth, its function in non-neuronal cells is not known. Therefore, this study was undertaken to explore the role of Cdk5 in the lens. Results showed that, within the adult mouse lens, Cdk5 was localized to the cytoplasm,especially along the lateral membranes of differentiating primary fiber cells,which suggests a role in cell-cell adhesion. Staining at the tips of elongating fiber cells was also particularly strong, suggesting a role in cell-matrix adhesion. To examine the possible role of Cdk5 in lens epithelial cell adhesion, we stably transfected N/N1003A rabbit lens epithelial cells with cDNAs for Cdk5 or a dominant-negative mutation, Cdk5-T33. Attachment to a fibronectin matrix, as measured with substrate-coated cell adhesion strips,was increased by Cdk5 overexpression, while an equivalent overexpression of Cdk5-T33 had no effect. Cdk5 also increased the rate of cell attachment and spreading as measured by electric cell-substrate impedance sensing (ECIS). In addition, Cdk5 overexpression decreased cell-cell adhesion as measured by a cell aggregation assay. These findings suggest that Cdk5 plays a role in regulating both cell-matrix and cell-cell interactions in the lens.

scholarly journals Cell-matrix adhesion and cell-cell adhesion differentially control basal myosin oscillation and Drosophila egg chamber elongation

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Xiang Qin ◽  
Byung Ouk Park ◽  
Jiaying Liu ◽  
Bing Chen ◽  
Valerie Choesmel-Cadamuro ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Egg Chamber ◽  
Cell Matrix Adhesion ◽  
Cell Cell

Regulation of cell???matrix adhesion and potentially also cell???cell adhesion by MIA

2006 ◽  
Vol 16 (Supplement 1) ◽  
pp. S18-S19
Author(s):  
A. Winklmeier ◽  
R. Bauer ◽  
S. Arndt ◽  
A. Bosserhoff
Keyword(s):  
Cell Adhesion ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion ◽  
Cell Cell

scholarly journals DISC1 regulates cell–cell adhesion, cell–matrix adhesion and neurite outgrowth

2010 ◽  
Vol 15 (8) ◽  
pp. 798-809 ◽  
Author(s):  
T Hattori ◽  
S Shimizu ◽  
Y Koyama ◽  
K Yamada ◽  
R Kuwahara ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Neurite Outgrowth ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion ◽  
Cell Cell

scholarly journals Keratin 6 regulates collective keratinocyte migration by altering cell–cell and cell–matrix adhesion

2018 ◽  
Vol 217 (12) ◽  
pp. 4314-4330 ◽  
Author(s):  
Fengrong Wang ◽  
Song Chen ◽  
Hans B. Liu ◽  
Carole A. Parent ◽  
Pierre A. Coulombe
Keyword(s):  
Cell Adhesion ◽  
Collective Cell Migration ◽  
Type Ii ◽  
Keratinocyte Migration ◽  
Cell Matrix ◽  
Interfollicular Epidermis ◽  
Migration Potential ◽  
Cell Matrix Adhesion ◽  
Cell Cell ◽  
Keratin 6

The a and b isoforms of keratin 6 (K6), a type II intermediate filament (IF) protein, are robustly induced upon injury to interfollicular epidermis. We previously showed that complete loss of K6a/K6b stimulates keratinocyte migration, correlating with enhanced Src activity. In this study, we demonstrate that this property is cell autonomous, depends on the ECM, and results from elevated speed, enhanced directionality, and an increased rate of focal adhesion disassembly. We show that myosin IIA interacts with K6a/K6b, that its levels are markedly reduced in Krt6a/Krt6b-null keratinocytes, and that inhibiting myosin ATPase activity normalizes the enhanced migration potential of Krt6a/Krt6b-null cells. Desmoplakin, which mediates attachment of IFs to desmosomes, is also expressed at reduced levels and is mislocalized to the nucleus in Krt6a/Krt6b-null cells, correlating with defects in cell adhesion. These findings reveal that K6a/K6b modulate keratinocyte migration by regulating cell–matrix and cell–cell adhesion and highlight a role for keratins in collective cell migration.

MATHEMATICAL MODELLING OF CANCER INVASION: THE IMPORTANCE OF CELL–CELL ADHESION AND CELL–MATRIX ADHESION

2011 ◽  
Vol 21 (04) ◽  
pp. 719-743 ◽  
Author(s):  
MARK A. J. CHAPLAIN ◽  
MIROSŁAW LACHOWICZ ◽  
ZUZANNA SZYMAŃSKA ◽  
DARIUSZ WRZOSEK
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cancer Cells ◽  
Classical Solutions ◽  
Invasion Process ◽  
Open Problems ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion ◽  
Cell Cell

The process of invasion of tissue by cancer cells is crucial for metastasis — the formation of secondary tumours — which is the main cause of mortality in patients with cancer. In the invasion process itself, adhesion, both cell–cell and cell–matrix, plays an extremely important role. In this paper, a mathematical model of cancer cell invasion of the extracellular matrix is developed by incorporating cell–cell adhesion as well as cell–matrix adhesion into the model. Considering the interactions between cancer cells, extracellular matrix and matrix degrading enzymes, the model consists of a system of reaction–diffusion partial integro–differential equations, with nonlocal (integral) terms describing the adhesive interactions between cancer cells and the host tissue, i.e. cell–cell adhesion and cell–matrix adhesion. Having formulated the model, we prove the existence and uniqueness of global in time classical solutions which are uniformly bounded. Then, using computational simulations, we investigate the effects of the relative importance of cell–cell adhesion and cell–matrix adhesion on the invasion process. In particular, we examine the roles of cell–cell adhesion and cell–matrix adhesion in generating heterogeneous spatio-temporal solutions. Finally, in the discussion section, concluding remarks are made and open problems are indicated.

scholarly journals Rap1GAP impairs cell-matrix adhesion in the absence of effects on cell-cell adhesion

2011 ◽  
Vol 5 (4) ◽  
pp. 323-331 ◽  
Author(s):  
Lisa A. Vuchak ◽  
Oxana M. Tsygankova ◽  
Judy L. Meinkoth
Keyword(s):  
Cell Adhesion ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion ◽  
Cell Cell

scholarly journals The cadherins: cell-cell adhesion molecules controlling animal morphogenesis

Development ◽  
1988 ◽  
Vol 102 (4) ◽  
pp. 639-655 ◽  
Author(s):  
M. Takeichi
Keyword(s):  
Cell Adhesion ◽  
Ectopic Expression ◽  
Amino Acid Sequences ◽  
Single Animal ◽  
Cell Layers ◽  
Dependent Cell ◽  
Cell Collective ◽  
Cell Cell

Cadherins are a family of glycoproteins involved in the Ca2+-dependent cell-cell adhesion mechanism which is detected in most kinds of tissues. Inhibition of the cadherin activity with antibodies induces dissociation of cell layers, indicating a fundamental importance of these molecules in maintaining the multicellular structure. Cadherins are divided into subclasses, including E-, N- and P-cadherins. While all subclasses are similar in molecular weight, Ca2+- and protease-sensitivity, each subclass is characterized by a unique tissue distribution pattern and immunological specificity. Analysis of amino acid sequences deduced from cDNA encoding these molecules showed that they are integral membrane proteins of 723–748 amino acids long and share common sequences; similarity in the sequences between subclasses is in a range of 50–60% when compared within a single animal species. L cells, with very little endogenous cadherin activity, transfected with the cadherin cDNA acquired high cadherin-mediated aggregating activity. Their colony morphology was altered by the ectopic expression of cadherins from the dispersed type to the compact type, providing direct evidence for a key role of cadherins in cell-cell adhesion. It has been suggested that cadherins bind cells by their homophilic interactions at the extracellular domain and are associated with actin bundles at the cytoplasmic domain. It appears that each cadherin subclass has binding specificity and this molecular family is involved in selective cell-cell adhesion. In development, the expression of each cadherin subclass is spatiotemporally regulated and associated with a variety of morphogenetic events; e.g. the termination or initiation of expression of a cadherin subclass in a given cell collective is correlated with its segregation from or connection with other cell collectives. Antibodies to cadherins were shown to perturb the morphogenesis of some embryonic organs in vitro. These observations suggest that cadherins play a crucial role in construction of tissues and the whole animal body.

Differential effects of histamine and thrombin on endothelial barrier function through actin-myosin tension

2002 ◽  
Vol 282 (1) ◽  
pp. H21-H29 ◽  
Author(s):  
Alan B. Moy ◽  
Ken Blackwell ◽  
Anant Kamath
Keyword(s):  
Cell Adhesion ◽  
Barrier Function ◽  
Umbilical Vein ◽  
Collagen Membrane ◽  
Tension Development ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Adhesion Sites ◽  
Cell Matrix Adhesion ◽  
Cell Cell

We compared temporal changes in isometric tension in cultured human umbilical vein endothelial cells inoculated on a polymerized collagen membrane with changes in cell-cell and cell-matrix adhesion derived by a mathematical model of transendothelial cell resistance. Thrombin and histamine disrupt barrier function by targeting a greater loss in cell-cell adhesion, which preceded losses in overall transendothelial resistance. There were minor losses in cell-matrix adhesion, which was temporally slower than the decline in the overall transendothelial resistance. In contrast, thrombin and histamine restored barrier function by initiating a restoration of cell-matrix adhesion, which occurred before an increase in overall transendothelial resistance. Thrombin mediated a second and slower decline in cell-cell adhesion, which was not observed in histamine-treated cells. This decline in cell-cell adhesion temporally correlated with expressed maximal levels of tension development, suggesting that actin-myosin contraction directly strains cell-cell adhesion sites. Pretreatment of cells with ML-7 mediated more rapid recovery of cell-cell adhesion and had no effect on cell-matrix adhesion. Taken together, expression of actin-myosin contraction affects the restoration of barrier function by straining cell-cell adhesion sites.

Sign in / Sign up

Export Citation Format

Share Document